Reshaping endoplasmic reticulum quality control through the unfolded protein response

Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including tissue-specific secretory proteomes, environmenta...

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Veröffentlicht in:	Molecular cell Jg. 82; H. 8; S. 1477
Hauptverfasser:	Wiseman, R Luke, Mesgarzadeh, Jaleh S, Hendershot, Linda M
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States 21.04.2022
Schlagworte:	Animals Endoplasmic Reticulum - metabolism Endoplasmic Reticulum Stress - genetics Mammals Quality Control Signal Transduction Unfolded Protein Response ERAD loss-of-function disease amyloid chaperone ER-associated degradation protein aggregation IRE1 PERK ATF6 protein misfolding disease XBP1s
ISSN:	1097-4164, 1097-4164
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Abstract	Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including tissue-specific secretory proteomes, environmental and genetic insults, and organismal aging, challenge ERQC. Thus, a key question is: how do cells adapt ERQC to match the diverse, ever-changing demands encountered during normal physiology and in disease? The answer lies in the unfolded protein response (UPR), a signaling mechanism activated by ER stress. In mammals, the UPR comprises three signaling pathways regulated downstream of the ER membrane proteins IRE1, ATF6, and PERK. Upon activation, these UPR pathways remodel ERQC to alleviate cellular stress and restore ER function. Here, we describe how UPR signaling pathways adapt ERQC, highlighting their importance for maintaining ER function across tissues and the potential for targeting the UPR to mitigate pathologies associated with protein misfolding diseases.
AbstractList	Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including tissue-specific secretory proteomes, environmental and genetic insults, and organismal aging, challenge ERQC. Thus, a key question is: how do cells adapt ERQC to match the diverse, ever-changing demands encountered during normal physiology and in disease? The answer lies in the unfolded protein response (UPR), a signaling mechanism activated by ER stress. In mammals, the UPR comprises three signaling pathways regulated downstream of the ER membrane proteins IRE1, ATF6, and PERK. Upon activation, these UPR pathways remodel ERQC to alleviate cellular stress and restore ER function. Here, we describe how UPR signaling pathways adapt ERQC, highlighting their importance for maintaining ER function across tissues and the potential for targeting the UPR to mitigate pathologies associated with protein misfolding diseases. Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including tissue-specific secretory proteomes, environmental and genetic insults, and organismal aging, challenge ERQC. Thus, a key question is: how do cells adapt ERQC to match the diverse, ever-changing demands encountered during normal physiology and in disease? The answer lies in the unfolded protein response (UPR), a signaling mechanism activated by ER stress. In mammals, the UPR comprises three signaling pathways regulated downstream of the ER membrane proteins IRE1, ATF6, and PERK. Upon activation, these UPR pathways remodel ERQC to alleviate cellular stress and restore ER function. Here, we describe how UPR signaling pathways adapt ERQC, highlighting their importance for maintaining ER function across tissues and the potential for targeting the UPR to mitigate pathologies associated with protein misfolding diseases.Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including tissue-specific secretory proteomes, environmental and genetic insults, and organismal aging, challenge ERQC. Thus, a key question is: how do cells adapt ERQC to match the diverse, ever-changing demands encountered during normal physiology and in disease? The answer lies in the unfolded protein response (UPR), a signaling mechanism activated by ER stress. In mammals, the UPR comprises three signaling pathways regulated downstream of the ER membrane proteins IRE1, ATF6, and PERK. Upon activation, these UPR pathways remodel ERQC to alleviate cellular stress and restore ER function. Here, we describe how UPR signaling pathways adapt ERQC, highlighting their importance for maintaining ER function across tissues and the potential for targeting the UPR to mitigate pathologies associated with protein misfolding diseases.
Author	Wiseman, R Luke Hendershot, Linda M Mesgarzadeh, Jaleh S
Author_xml	– sequence: 1 givenname: R Luke surname: Wiseman fullname: Wiseman, R Luke email: wiseman@scripps.edu organization: Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: wiseman@scripps.edu – sequence: 2 givenname: Jaleh S surname: Mesgarzadeh fullname: Mesgarzadeh, Jaleh S organization: Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 3 givenname: Linda M surname: Hendershot fullname: Hendershot, Linda M email: linda.hendershot@stjude.org organization: Department of Tumor Biology, St Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address: linda.hendershot@stjude.org
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Title	Reshaping endoplasmic reticulum quality control through the unfolded protein response
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